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  Structural basis of assembly chaperone- mediated snRNP formation.

Grimm, C., Chari, A., Pelz, J. P., Kuper, J., Kisker, C., Diederichs, K., et al. (2013). Structural basis of assembly chaperone- mediated snRNP formation. Molecular Cell, 49(4), 692-703. doi:10.1016/j.molcel.2012.12.009.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000E-F667-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-1D65-3
Genre: Journal Article

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Grimm, C., Author
Chari, A., Author
Pelz, J. P., Author
Kuper, J., Author
Kisker, C., Author
Diederichs, K., Author
Stark, H.1, Author              
Schindelin, H., Author
Fischer, U., Author
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1Research Group of 3D Electron Cryo-Microscopy, MPI for biophysical chemistry, Max Planck Society, ou_578577              

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 Abstract: Small nuclear ribonucleoproteins (snRNPs) represent key constituents of major and minor spliceosomes. snRNPs contain a common core, composed of seven Sm proteins bound to snRNA, which forms in a step-wise and factor-mediated reaction. The assembly chaperone pICln initially mediates the formation of an otherwise unstable pentameric Sm protein unit. This so-called 6S complex docks subsequently onto the SMN complex, which removes pICln and enables the transfer of pre-assembled Sm proteins onto snRNA. X-ray crystallography and electron microscopy was used to investigate the structural basis of snRNP assembly. The 6S complex structure identifies pICln as an Sm protein mimic, which enables the topological organization of the Sm pentamer in a closed ring. A second structure of 6S bound to the SMN complex components SMN and Gemin2 uncovers a plausible mechanism of pICln elimination and Sm protein activation for snRNA binding. Our studies reveal how assembly factors facilitate formation of RNA-protein complexes in vivo.

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Language(s): eng - English
 Dates: 2013-01-17
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.molcel.2012.12.009
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Title: Molecular Cell
Source Genre: Journal
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Pages: - Volume / Issue: 49 (4) Sequence Number: - Start / End Page: 692 - 703 Identifier: -